title: Perfluorodecanoic acid binding to hemoproteins: new insights from spectroscopic studies.
abstract: Perfluorodecanoic acid (PFDA), a representative of the perfluoroalkyl acids, poses a great threat to humans and animals via food and other potential sources. In this work, we determined the effects of PFDA binding to two hemoproteins, bovine hemoglobin (BHb) and myoglobin (Mb). Using fluorescence spectroscopy, we found that PFDA greatly enhanced the fluorescence intensity of both hemoproteins, while perfluorooctanoic acid (PFOA) and perfluoropentanoic acid (PFPA) have minimal effects on the fluorescence. UV-vis absorption (UV) spectroscopy showed that PFDA induced the unfolding of the hemoproteins accompanied by exposure of the heme pocket and facilitating the formation of hemichrome. Additionally, as shown by the circular dichroism (CD) data, PFDA altered the secondary structure of both BHb and Mb. This work elucidates the interaction mechanism of PFDA with two hemoproteins.
authors.affiliation: Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment & Health, Shandong Province, 27# Shanda South Road, Jinan 250100, PR China.
authors.forename: Pengfei
authors.initials: P
authors.lastname: Qin
authors.forename: Rutao
authors.initials: R
authors.lastname: Liu
authors.forename: Yue
authors.initials: Y
authors.lastname: Teng
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003652:Decanoic Acids / Q000378:metabolism*; D005466:Fluorocarbons / Q000378:metabolism*; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D006736:Horses; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013057:Spectrum Analysis
chemical_list: D003652:Decanoic Acids; D005466:Fluorocarbons; D006454:Hemoglobins; D009211:Myoglobin; C036567:perfluorodecanoic acid